Q9MZT9 · MYC_TUPGL

Function

function

Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity).
Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular FunctionE-box binding
Molecular Functionprotein dimerization activity
Molecular Functionprotein-containing complex binding
Biological Processchromatin remodeling
Biological Processchromosome organization
Biological ProcessDNA damage response
Biological ProcessG1/S transition of mitotic cell cycle
Biological Processintracellular iron ion homeostasis
Biological ProcessMAPK cascade
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of cell division
Biological Processnegative regulation of monocyte differentiation
Biological Processnegative regulation of stress-activated MAPK cascade
Biological Processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of epithelial cell proliferation
Biological Processpositive regulation of fibroblast proliferation
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of DNA-templated transcription
Biological Processregulation of somatic stem cell population maintenance
Biological Processregulation of telomere maintenance
Biological Processresponse to gamma radiation
Biological Processresponse to xenobiotic stimulus

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Myc proto-oncogene protein
  • Alternative names
    • Proto-oncogene c-Myc
    • Transcription factor p64

Gene names

    • Name
      MYC

Organism names

Accessions

  • Primary accession
    Q9MZT9

Subcellular Location

Keywords

Phenotypes & Variants

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, cross-link, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00001273041-439Myc proto-oncogene protein
Modified residue6Phosphoserine
Cross-link52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue58Phosphothreonine; by GSK3; alternate
Glycosylation58O-linked (GlcNAc) threonine; alternate
Modified residue62Phosphoserine; by DYRK2, GSK3 and CDK2
Modified residue71Phosphoserine
Modified residue143N6-acetyllysine; by PCAF; alternate
Cross-link143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue148N6-acetyllysine; alternate
Cross-link148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue157N6-acetyllysine; by PCAF
Modified residue161Phosphoserine
Modified residue275N6-acetyllysine; by PCAF
Modified residue293Phosphoserine
Cross-link298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue317N6-acetyllysine; by PCAF
Modified residue323N6-acetyllysine; by PCAF
Modified residue329Phosphoserine; by PIM2; in vitro
Modified residue371N6-acetyllysine; by PCAF

Post-translational modification

Phosphorylated by PRKDC (By similarity).
Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity).
Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity).
Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRPC4AP) complex. Ubiquitinated by UBR5 when not forming a heterodimer with another bHLH protein, leading to its degradation: UBR5 recognizes and binds a degron that is only available upon heterodimer dissociation (By similarity).
Ubiquitinated by TRIM6 in a phosphorylation-independent manner

Keywords

PTM databases

Interaction

Subunit

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (By similarity).
Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity).
Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (By similarity).
Interacts with CIP2A; leading to the stabilization of MYC (By similarity).
Interacts with NUP205 (By similarity).

Structure

Family & Domains

Features

Showing features for motif, region, compositional bias, domain.

TypeIDPosition(s)Description
Motif100-1089aaTAD
Region203-359Disordered
Compositional bias206-233Polar residues
Compositional bias345-359Basic and acidic residues
Domain354-406bHLH
Motif355-364UBR5-degron
Region413-434Leucine-zipper

Domain

The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    439
  • Mass (Da)
    48,543
  • Last updated
    2000-10-01 v1
  • Checksum
    C98C5AFCD8897E1D
MPLNVSFASRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVASFSPRGDDDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPSPARGHSGCSTSSLYLQDLSAAASECIDPSVVFPYPLNDGSSPKPCASPDSTAFSPSSDSLLSSTESSPRASPEPLALHEETPPTTSSDSEEDQEDEEEIDVVSVEKRQPPTKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCASPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEKDLLRKRREQLKHKLEQLRNSCA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias206-233Polar residues
Compositional bias345-359Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF160485
EMBL· GenBank· DDBJ
AAF80394.1
EMBL· GenBank· DDBJ
Genomic DNA
AF160484
EMBL· GenBank· DDBJ
AAF80394.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp